2jiz
From Proteopedia
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- | [[Image: | + | ==THE STRUCTURE OF F1-ATPASE INHIBITED BY RESVERATROL.== |
+ | <StructureSection load='2jiz' size='340' side='right' caption='[[2jiz]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | [[2jiz]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JIZ OCA]. <br> | ||
+ | <b>Related:</b> [[1bmf|1bmf]], [[1cow|1cow]], [[1e1q|1e1q]], [[1e1r|1e1r]], [[1e79|1e79]], [[1efr|1efr]], [[1h8e|1h8e]], [[1h8h|1h8h]], [[1nbm|1nbm]], [[1ohh|1ohh]], [[1qo1|1qo1]], [[1w0j|1w0j]], [[1w0k|1w0k]], [[2ck3|2ck3]], [[2jdi|2jdi]], [[2uys|2uys]]<br> | ||
+ | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ji/2jiz_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The structures of F(1)-ATPase from bovine heart mitochondria inhibited with the dietary phytopolyphenol, resveratrol, and with the related polyphenols quercetin and piceatannol have been determined at 2.3-, 2.4- and 2.7-A resolution, respectively. The inhibitors bind to a common site in the inside surface of an annulus made from loops in the three alpha- and three beta-subunits beneath the "crown" of beta-strands in their N-terminal domains. This region of F(1)-ATPase forms a bearing to allow the rotation of the tip of the gamma-subunit inside the annulus during catalysis. The binding site is a hydrophobic pocket between the C-terminal tip of the gamma-subunit and the beta(TP) subunit, and the inhibitors are bound via H-bonds mostly to their hydroxyl moieties mediated by bound water molecules and by hydrophobic interactions. There are no equivalent sites between the gamma-subunit and either the beta(DP) or the beta(E) subunit. The inhibitors probably prevent both the synthetic and hydrolytic activities of the enzyme by blocking both senses of rotation of the gamma-subunit. The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis. | ||
- | + | Mechanism of inhibition of bovine F1-ATPase by resveratrol and related polyphenols.,Gledhill JR, Montgomery MG, Leslie AG, Walker JE Proc Natl Acad Sci U S A. 2007 Aug 21;104(34):13632-7. Epub 2007 Aug 13. PMID:17698806<ref>PMID:17698806</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Gledhill, J R.]] | [[Category: Gledhill, J R.]] |
Revision as of 08:27, 30 April 2014
THE STRUCTURE OF F1-ATPASE INHIBITED BY RESVERATROL.
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